6WAT

complex structure of PHF1

This is a non-PDB format compatible entry.

Summary for 6WAT

• Entry DOI: 10.2210/pdb6wat/pdb
• Descriptor: PHD finger protein 1, Histone H3.1t peptide, UNKNOWN ATOM OR ION, ... (4 entities in total)
• Functional Keywords: phf1, tudor, histone variant, complex, structural genomics, structural genomics consortium, sgc, gene regulation
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 60
• Total formula weight: 238712.40

Authors

Dong, C.,Bountra, C.,Edwards, A.M.,Arrowsmith, C.H.,Min, J.R.,Structural Genomics Consortium (SGC) (deposition date: 2020-03-26, release date: 2020-08-26, Last modification date: 2023-10-18)

Primary citation

Dong, C.,Nakagawa, R.,Oyama, K.,Yamamoto, Y.,Zhang, W.,Dong, A.,Li, Y.,Yoshimura, Y.,Kamiya, H.,Nakayama, J.I.,Ueda, J.,Min, J.
Structural basis for histone variant H3tK27me3 recognition by PHF1 and PHF19.
Elife, 9:-, 2020

PubMed Abstract: The Polycomb repressive complex 2 (PRC2) is a multicomponent histone H3K27 methyltransferase complex, best known for silencing the genes during embryonic development. The Polycomb-like proteins PHF1, MTF2, and PHF19 are critical components of PRC2 by stimulating its catalytic activity in embryonic stem cells. The Tudor domains of PHF1/19 have been previously shown to be readers of H3K36me3 in vitro. However, some other studies suggest that PHF1 and PHF19 co-localize with the H3K27me3 mark but not H3K36me3 in cells. Here, we provide further evidence that PHF1 co-localizes with H3t in testis and its Tudor domain preferentially binds to H3tK27me3 over canonical H3K27me3 in vitro. Our complex structures of the Tudor domains of PHF1 and PHF19 with H3tK27me3 shed light on the molecular basis for preferential recognition of H3tK27me3 by PHF1 and PHF19 over canonical H3K27me3, implicating that H3tK27me3 might be a physiological ligand of PHF1/19.

PubMed: 32869745
DOI: 10.7554/eLife.58675

Experimental method

X-RAY DIFFRACTION (1.8 Å)